Silicon Investor (SI) -- The First Internet Community

STOCKTALK

We've detected that you're using an ad content blocking browser plug-in or feature. Ads provide a critical source of revenue to the continued operation of Silicon Investor. We ask that you disable ad blocking while on Silicon Investor in the best interests of our community. If you are not using an ad blocker but are still receiving this message, make sure your browser's tracking protection is set to the 'standard' level.

Biotech / Medical : XOMA. Bull or Bear? -- Ignore unavailable to you. Want to Upgrade?

To: Robert K. who wrote (7499)	10/18/1998 11:51:00 AM
From: aknahow	Respond to of 17367

Bob, thanks, I think, I had help from you and your message which mentioned ING several times. Parse that! Then I did search on the IBM site., for XOMA and ING. This patent was issued in 1996. Xoma has several old things floating around that seem interesting but which I expect XOMA can't focus on at this time. My favorite is Thaumitin (sp) or the artificial sweetner. I see MTC is proceeding to develop its' own which is 6 to 8 thousand times sweeter than sugar and will compete with its' own Nutrasweet, which is only 100 to 200 times as sweet.

To: Robert K. who wrote (7499)	10/19/1998 12:33:00 AM
From: aknahow	Respond to of 17367

Bob, while old I think this URL reinforces the concept that there is a lot of interest in BPI. pctvmag.com Any comments on the above would be appreciated.

To: Robert K. who wrote (7499)	10/19/1998 1:08:00 AM
From: aknahow	Read Replies (1) \| Respond to of 17367

Title SALMONELLA TYPHIMURIUM RESPONSES TO A BACTERICIDAL PROTEIN FROM HUMAN NEUTROPHILS Journal Molecular Microbiology. 17(3):523-531, 1995 Aug. ISSN 0950-382X ABS Bactericidal/permeability-increasing protein [BPI] is a cationic antimicrobial protein from neutrophils that specifically binds to the surfaces of Gram-negative bacteria via the lipid A component of lipopolysaccharide. To obtain information about the responses of Salmonella typhimurium to cell-surface damage by BPI, two-dimensional gel electrophoresis and N-terminal microsequencing were used to identify proteins that were induced or repressed following BPI treatment. The majority of the affected proteins are involved in central metabolic processes. Upon addition of BPI, the beta-subunit of the F-1 portion of Escherichia coil ATP synthase was repressed threefold whereas six proteins were induced up to 11-fold. Three of the latter were identified as lipoamide dehydrogenase, enoyl-acyl carrier protein reductase, and the heat-shock protein HtpG. Additionally, a novel protein, BipA, was identified that is induced over sevenfold by BPI; sequence analysis suggests that it belongs to the GTPase superfamily and interacts with ribosomes. A conserved direct-repeat motif is present in the regulatory regions of several BPI-inducible genes, including the bipA gene. Only one of the BPI-responsive proteins was induced when cells were treated with polymyxin B, which also binds to lipid A. We therefore conclude that BPI and polymyxin B affect different global regulatory networks in S. typhimurium even though they bind with high affinity to the same cell-surface component. [References: 4 Bob and everyone: There are several references, or rather at least two. This is the one I had not seen before.

To: Robert K. who wrote (7499)	10/19/1998 12:47:00 PM
From: aknahow	Respond to of 17367

Really want to know if XOMA has any potential role in this area. I do not know if they do and am not in anyway implying that they do. Curr Opin Lipidol 1998 Jun;9(3):203-9 Structure and function of the plasma phospholipid transfer protein. Lagrost L, Desrumaux C, Masson D, Deckert V, Gambert P Lipoprotein Biochemistry Laboratory, INSERM U498, Department of Medicine, Dijon, France. Recent cloning and sequencing of plasma phospholipid transfer protein complementary DNA revealed that phospholipid transfer protein belongs to the lipid transfer/lipopolysaccharide binding protein family that includes the cholesteryl ester transfer protein, the bactericidal permeability increasing protein and the lipopolysaccharide-binding protein. In addition to structural similarities, members of the lipid transfer/lipopolysaccharide-binding protein family might share some common functional properties, and recent studies demonstrated that phospholipid transfer protein can act in several distinct metabolic processes. In particular, the molecular transfer of phospholipids, unesterified cholesterol, alpha-tocopherol and lipopolysaccharides by phospholipid transfer protein suggests that it might be involved both in lipoprotein metabolism and in antimicrobial defence, resulting in a growing interest in this protein. Publication Types:

To: Robert K. who wrote (7499)	10/19/1998 1:10:00 PM
From: aknahow	Respond to of 17367

Same question but more information. To me it sounds like, disorder the surface and then tuck it in pocket and carry it away??? <g> Curr Opin Struct Biol 1998 Aug;8(4):426-34 The implications of the structure of the bactericidal/permeability-increasing protein on the lipid-transfer function of the cholesteryl ester transfer protein. Bruce C, Beamer LJ, Tall AR Department of Medicine, Columbia University, New York, NY 10032, USA. cb34@columbia.edu [Medline record in process] The cholesteryl ester transfer protein (CETP) is evolutionarily related to the bactericidal/permeability-increasing protein (BPI). The recently solved structure of BPI shows an elongated, boomerang-shaped molecule, with two hydrophobic pockets opening to its concave side. These pockets each contain a phospholipid molecule. A model of CETP, based on the recently solved crystal structure of BPI, provides the basis for interpreting functional studies on CETP. In this model, C-terminal residues 461-476, which were shown to be required for neutral lipid transfer between plasma lipoproteins, from an amphipathic helix covering the opening of the N-terminal pocket. A possible lipid-transfer mechanism for CETP, with the initial step involving the disordering of lipids in the lipoprotein surface, followed by the flipping and entry of a lipid molecule into the hydrophobic lipid-binding pocket, is hypothesized in light of structural evidence and recent studies.

To: Robert K. who wrote (7499)	10/20/1998 12:06:00 AM
From: aknahow	Respond to of 17367

One more document on LBP BPI CETP * LBP / BPI / CETP family signature * ************************************* A family of serum glycoproteins that binds to lipids has recently [1,2] been recognized. This family groups together: - Lipopolysaccharide-binding protein (LBP). LBP binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. The LBP/LPS complex seems to interact with the CD14 receptor and may be responsible for the secretion of alpha-TNF. - Bactericidal permeability-increasing protein (BPI). Like LBP, BPI binds LPS and has a cytotoxic activity on Gram-negative bacteria. - Cholesteryl ester transfer protein (CETP). CETP is involved in the transfer of insoluble cholesteryl esters in reverse cholesterol transport. These proteins are structurally related and share many regions of sequence similarities. As a signature pattern we have selected one of these regions, which is located in the N-terminal section of these proteins; a region which could be involved in the binding to the lipids [2]. -Consensus pattern: G-[LIVM](2)-x-R-I-[ST]-x(3)-L-x(5)-[EQ]-x(4)-[LIVM]-Q- x(8)-P -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in SWISS-PROT: NONE. -Last update: May 1991 / Text revised. [ 1] Schumann R.R., Leong S.R., Flaggs G.W., Gray P.W., Wright S.D., Mathison J.C., Tobias P.S., Ulevitch R.J. Science 249:1429-1431(1990). [ 2] Gray P.W., Flaggs G., Leong S.R., Gumina R.J., Weiss J., Ooi C.E., Elsbach P. J. Biol. Chem. 264:9505-9509(19

To: Robert K. who wrote (7499)	10/21/1998 1:10:00 AM
From: aknahow	Read Replies (1) \| Respond to of 17367

Deep background on fungicides. My quick read is a common problem is toxic nature and difficulty in crossing membranes to get to the target. vet.purdue.edu BTW since Biostock always thought there was a future in treating animals I did not let the DVM source bother me.<g>